Journal of Biological Chemistry
Volume 289, Issue 50, 12 December 2014, Pages 34620-34626
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Molecular Biophysics
Interaction of the Intermembrane Space Domain of Tim23 Protein with Mitochondrial Membranes*

https://doi.org/10.1074/jbc.M114.595702Get rights and content
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Tim23 mediates protein translocation into mitochondria. Although inserted into the inner membrane, the dynamic association of its intermembrane space (IMS) domain with the outer membrane promotes protein import. However, little is known about the molecular basis of this interaction. Here, we demonstrate that the IMS domain of Tim23 tightly associates with both inner and outer mitochondrial membrane-like membranes through a hydrophobic anchor at its N terminus. The structure of membrane-bound Tim23IMS is highly dynamic, allowing recognition of both the incoming presequence and other translocase components at the translocation contact. Cardiolipin enhances Tim23 membrane attachment, suggesting that cardiolipin can influence preprotein import.

Lipid
Membrane
Mitochondria
Nuclear Magnetic Resonance (NMR)
Protein Translocation
Protein Import

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*

This work was supported by Deutsche Forschungsgemeinschaft Collaborative Research Center 860 Project B2 (to M. Z.).

1

Both authors contributed equally to this work.